The cover . . .

Wrinch Discusses Proteins in Stieglitz Lecture

A S T A F F R E P O R T

A HKORIES of protein s t ructure were dis­cussed b y Dorothy Wrinch, of Smith College, a s the Stieglitz Memorial Lec­turer Jan. 24. The lecture was held in Pat ton Gymnas ium, Northwestern Uni­versity, Kvanston, 111., as the conclusion of t he second all-day Technical Confer­ence of t h e Chicago Section of the A M E R I ­CAN C HE MIC AL SOCIETY. II . K. Summer-bell, of Northwestern Universi ty and chairman of the Chicago Section, presided a t t he meeting, and Β . Β. Freud, of Illinois Inst i tute of Tech­nology, introduced the lecturer. Dr. Freud was a close friend of Stieglitz and served as treas­urer in establishing the Stieglitz lec­tureship fund. Nearly 500 at­tended t h e lecture.

Announcing as Β. Β. Freud her premise t h a t protein is an enti ty, Dr. Wrinch reviewed evidence to support this view and concluded that recent work in physical chemistry and chemical crystal­lography yields a definite and precise picture of the s t ructure of nat ive protein.

T h e instabi l i ty of the protein molecule, or proteon, apparent ly resides in the skele­ton, asserted D r . Wrinch. Each proteon maintains its existence only in vir tue of the associations of favorably juxtaposed R-subst i tuents . Th i s precarious stability may be intramolecular or it may depend also on some intermolecular R-group as­sociations.

T h e proteon skeleton, though unstable, is rigid. In this w a y associations of R-groups which, are configurationally defi­nite are made possible.

T h e protein character resides in the ex­tremely well-defined, though a t present unknown, s t ructure of proteon skeletons. "This , w e expect, will prove to be as defi­nite an en t i ty as the carbon skeleton of the sterols or the carbon-nitrogen skeleton of hexamethylene te t ramine. Alternatively it may t u r n o u t to be a homologous series of ent i t ies , each of this degree of dennite-ness, embodying some common construc­tional principle."

T h e part icular composition of an indi­vidual pro teon resides in the particular numbers of individual R-groups (alanines, arginines, etc.) among its subst i tuents .

T h e fact t h a t definite configurations of R-group associations are the common fac­tor in fundamental phenomena of enzy-

mology, immunology, pharmacology, and other fields of protein studies makes it appear likely tha t this same factor may throw light on the nature of biosynthesis of protein molecules.

The Lecturer

Dorothy Wrinch, mathematician, chem­ist, a n d biologist, was born in Argentina and educated in England and o n the Con­t inent . She holds degrees from Cam­bridge, London University, and Oxford where she was a member of t h e faculty of physical sciences for many years.

In 1935, Dr. Wrinch came to the United States at the invitation of the Rockefeller Foundation which until 1941 sponsored her new studies in the application of mathe­matics to structure problems of biology and medicine. In 1939 she became lec­turer in chemistry a t Johns Hopkins Uni­versity, leaving in 1941 t o become visiting professor a t Amherst, M t . Holyoke, and Smith Colleges. Since 1942 she has been lecturing in the physics department of Smith College with her summer activities centered nt the Woods Hole Marine Bio-

Darothy Wrinch

logical Laboratory. In 1943 she became an American citizen.

Dr. Wrinch is the wife of O. C. Glaser, professor of biology at Amherst College. Her daughter is a junior at the University of Michigan.

Dr. Wrinch/s work has covered a wide field, mainly pure mathematics, mathe­matical physics, and probability theory. Since 1934 she has been mainly concerned with theoretical chemistry, particularly nat ive proteins, and molecular biology; most recently, crystallography.

The Stieglitz Lecture A HE STIEGLITZ lectureship, founded

in 1940 by the Chicago Section of the AMERICAN CHEMICAL SOCIETY and the alumni of the chemistry department of t h e University of Chicago, honors the memory of Jul­ius Stieglitz, dis-t i n g u i s h e d chemist and professor, and symbolizes the breadth of his interest in sci­ence and the ar t s . The lec­turer is chosen b y the university to speak in a field of chemistry related t o those in which Stieglitz worked. T h e lecture is alter­nated annually between t h e Chicago Section and the university.

Stieglitz' work in organic chemistry embraced several interrelated fields and is described in 66 research papers a n d the theses of U S doctors who took their degrees with him. I n addition, Stieglitz will long b e remembered for h i s contributions to analytical chemis­

try and for his lucid and meticulous lectures.

Stieglitz was born in Hoboken, N. J. , in 1867. His boyhood and elementary schooling were passed in New York City, and at the age of 14 his family took him and his brothers to Germany to complete their education.

Returning t o this country in 1890, Stieglitz worked for two years as a toxi-cologist with Parke , Davis and Co. but went to the University of Chicago as docent under Kef in 1S92. He rose t o professor in 1905, chairman of the chemistry depar tment in 1915.

An exponent of chemotherapeutic research, Stieglitz' lifelong interest in medicine found expression in his vice chairmanship of the Council of Phar­macy and Chemistry of the American Medical Association, 1905-24, and his editorship of "Chemistry in Medicine", published by t h e Chemical Foundation. Recipient of many honors, Stieglitz was president of t h e AMERICAN CHEMICAL SOCIETY in 1917. Retiring in 1933, Steiglitz continued his work as emeritus professor unt i l his death, Jan . 10, 1937.

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